NHOA_SALTY
ID NHOA_SALTY Reviewed; 281 AA.
AC Q00267;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arylamine N-acetyltransferase / N-hydroxyarylamine O-acetyltransferase {ECO:0000303|PubMed:10876241, ECO:0000303|PubMed:1569093};
DE EC=2.3.1.118 {ECO:0000269|PubMed:1569093, ECO:0000269|PubMed:7889864};
DE EC=2.3.1.5 {ECO:0000269|PubMed:1569093, ECO:0000269|PubMed:7889864};
DE AltName: Full=Arylhydroxamate N,O-acetyltransferase {ECO:0000305};
DE AltName: Full=NAT101;
GN Name=nhoA; OrderedLocusNames=STM1582;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF CYS-69, AND ACTIVE SITE.
RX PubMed=1569093; DOI=10.1016/s0021-9258(18)42462-3;
RA Watanabe M., Sofuni T., Nohmi T.;
RT "Involvement of Cys69 residue in the catalytic mechanism of N-
RT hydroxyarylamine O-acetyltransferase of Salmonella typhimurium. Sequence
RT similarity at the amino acid level suggests a common catalytic mechanism of
RT acetyltransferase for S. typhimurium and higher organisms.";
RL J. Biol. Chem. 267:8429-8436(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND ACTIVE SITE.
RC STRAIN=ATCC 29631 / TA 1538;
RX PubMed=7889864; DOI=10.2307/3432157;
RA Watanabe M., Igarashi T., Kaminuma T., Sofuni T., Nohmi T.;
RT "N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium: proposal
RT for a common catalytic mechanism of arylamine acetyltransferase enzymes.";
RL Environ. Health Perspect. 102:83-89(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT STRUCTURE, AND ACTIVE SITES.
RX PubMed=10876241; DOI=10.1038/76783;
RA Sinclair J.C., Sandy J., Delgoda R., Sim E., Noble M.E.M.;
RT "Structure of arylamine N-acetyltransferase reveals a catalytic triad.";
RL Nat. Struct. Biol. 7:560-564(2000).
CC -!- FUNCTION: Catalyzes both the acetyl-CoA-dependent N-acetylation of
CC aromatic amines and the O-acetylation of N-hydroxyarylamines. In vitro,
CC catalyzes the O-acetylation of N-hydroxy-Glu-P-1, and the N-acetylation
CC of isoniazid and 2-aminofluorene. {ECO:0000269|PubMed:1569093,
CC ECO:0000269|PubMed:7889864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an arylamine = an N-acetylarylamine + CoA;
CC Xref=Rhea:RHEA:16613, ChEBI:CHEBI:13790, ChEBI:CHEBI:50471,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.5;
CC Evidence={ECO:0000269|PubMed:1569093, ECO:0000269|PubMed:7889864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an N-hydroxyarylamine = an N-acetoxyarylamine +
CC CoA; Xref=Rhea:RHEA:20277, ChEBI:CHEBI:13792, ChEBI:CHEBI:21494,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.118;
CC Evidence={ECO:0000269|PubMed:1569093, ECO:0000269|PubMed:7889864};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and iodoacetamide.
CC {ECO:0000269|PubMed:1569093, ECO:0000269|PubMed:7889864}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for acetyl-CoA (in the presence of N-hydroxy-Glu-P-1)
CC {ECO:0000269|PubMed:1569093};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:10876241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1569093,
CC ECO:0000269|PubMed:7889864}.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D90301; BAA14331.1; -; Genomic_DNA.
DR EMBL; S76130; AAB33787.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20500.1; -; Genomic_DNA.
DR PIR; A38090; A38090.
DR RefSeq; NP_460541.1; NC_003197.2.
DR RefSeq; WP_000200329.1; NC_003197.2.
DR PDB; 1E2T; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-281.
DR PDBsum; 1E2T; -.
DR AlphaFoldDB; Q00267; -.
DR SMR; Q00267; -.
DR STRING; 99287.STM1582; -.
DR PaxDb; Q00267; -.
DR EnsemblBacteria; AAL20500; AAL20500; STM1582.
DR GeneID; 1253100; -.
DR KEGG; stm:STM1582; -.
DR PATRIC; fig|99287.12.peg.1673; -.
DR HOGENOM; CLU_049918_1_1_6; -.
DR OMA; CYEHNTL; -.
DR PhylomeDB; Q00267; -.
DR BioCyc; SENT99287:STM1582-MON; -.
DR BRENDA; 2.3.1.5; 5542.
DR SABIO-RK; Q00267; -.
DR EvolutionaryTrace; Q00267; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046990; F:N-hydroxyarylamine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001447; Arylamine_N-AcTrfase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR11786; PTHR11786; 1.
DR Pfam; PF00797; Acetyltransf_2; 1.
DR PRINTS; PR01543; ANATRNSFRASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..281
FT /note="Arylamine N-acetyltransferase / N-hydroxyarylamine
FT O-acetyltransferase"
FT /id="PRO_0000107916"
FT ACT_SITE 69
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:10876241,
FT ECO:0000305|PubMed:1569093, ECO:0000305|PubMed:7889864"
FT ACT_SITE 107
FT /evidence="ECO:0000305|PubMed:10876241"
FT ACT_SITE 122
FT /evidence="ECO:0000305|PubMed:10876241"
FT MUTAGEN 69
FT /note="C->A: Loss of O- and N-acetyltransferase
FT activities."
FT /evidence="ECO:0000269|PubMed:1569093"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1E2T"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 157..174
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1E2T"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:1E2T"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1E2T"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:1E2T"
SQ SEQUENCE 281 AA; 32178 MW; 5FB3B667BD4D7804 CRC64;
MTSFLHAYFT RLHCQPLGVP TVEALRTLHL AHNCAIPFEN LDVLLPREIQ LDETALEEKL
LYARRGGYCF ELNGLFERAL RDIGFNVRSL LGRVILSHPA SLPPRTHRLL LVDVEDEQWI
ADVGFGGQTL TAPLRLQAEI AQQTPHGEYR LMQEGSTWIL QFRHHEHWQS MYCFDLGVQQ
QSDHVMGNFW SAHWPQSHFR HHLLMCRHLP DGGKLTLTNF HFTRYHQGHA VEQVNVPDVP
SLYQLLQQQF GLGVNDVKHG FTEAELAAVM AAFDTHPEAG K
